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Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes.

Viens P, Lacombe-Harvey MÈ, Brzezinski R - Mar Drugs (2015)

Bottom Line: Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan.Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level.This review is focused on the taxonomic distribution of GH46 proteins, their multi-modular character, the structure-function relationships and their biological functions in the host organisms.

View Article: PubMed Central - PubMed

Affiliation: Biologie, Faculté des Sciences, Université de Sherbrooke, 2500, boul. de l'Université, Sherbrooke, QC J1K 2R1, Canada. Pascal.Viens@USherbrooke.ca.

ABSTRACT
Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan. Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level. They were also subjected to numerous site-directed mutagenesis studies, unraveling the molecular mechanisms of hydrolysis. This review is focused on the taxonomic distribution of GH46 proteins, their multi-modular character, the structure-function relationships and their biological functions in the host organisms.

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Percentages of identity (in bold) and similarity (into brackets) among the primary amino acid sequences of the catalytic modules of the best characterized chitosanases from clusters A–D. CHIS_BACCI: chitosanase from Bacillus circulans MH-K1; CsnN174: chitosanase from Streptomyces sp. N174; BSU26890: chitosanase from Bacillus subtilis 168; Q84608_PBCV1: chitosanase from Chlorella virus 1 of Paramecium bursaria. The sequences were aligned pairwise with Clustal Omega [26]. Identity and similarity were determined using the SIAS server (http://imed.med.ucm.es/Tools/sias.html).
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marinedrugs-13-06566-f002: Percentages of identity (in bold) and similarity (into brackets) among the primary amino acid sequences of the catalytic modules of the best characterized chitosanases from clusters A–D. CHIS_BACCI: chitosanase from Bacillus circulans MH-K1; CsnN174: chitosanase from Streptomyces sp. N174; BSU26890: chitosanase from Bacillus subtilis 168; Q84608_PBCV1: chitosanase from Chlorella virus 1 of Paramecium bursaria. The sequences were aligned pairwise with Clustal Omega [26]. Identity and similarity were determined using the SIAS server (http://imed.med.ucm.es/Tools/sias.html).

Mentions: It thus appears that GH46 chitosanases from actinobacteria are rather homogenous at the primary sequence level, being grouped essentially in one large cluster A, while chitosanases from Firmicutes (Bacillus and related genera) fall into two distinct groups, one of which (cluster B) is relatively closer to the actinobacterial proteins than the other (cluster D). This is illustrated in Figure 2, showing the percentages of identity and similarity among the sequences of the catalytic modules of the best-characterized chitosanases from each cluster.


Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes.

Viens P, Lacombe-Harvey MÈ, Brzezinski R - Mar Drugs (2015)

Percentages of identity (in bold) and similarity (into brackets) among the primary amino acid sequences of the catalytic modules of the best characterized chitosanases from clusters A–D. CHIS_BACCI: chitosanase from Bacillus circulans MH-K1; CsnN174: chitosanase from Streptomyces sp. N174; BSU26890: chitosanase from Bacillus subtilis 168; Q84608_PBCV1: chitosanase from Chlorella virus 1 of Paramecium bursaria. The sequences were aligned pairwise with Clustal Omega [26]. Identity and similarity were determined using the SIAS server (http://imed.med.ucm.es/Tools/sias.html).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4663542&req=5

marinedrugs-13-06566-f002: Percentages of identity (in bold) and similarity (into brackets) among the primary amino acid sequences of the catalytic modules of the best characterized chitosanases from clusters A–D. CHIS_BACCI: chitosanase from Bacillus circulans MH-K1; CsnN174: chitosanase from Streptomyces sp. N174; BSU26890: chitosanase from Bacillus subtilis 168; Q84608_PBCV1: chitosanase from Chlorella virus 1 of Paramecium bursaria. The sequences were aligned pairwise with Clustal Omega [26]. Identity and similarity were determined using the SIAS server (http://imed.med.ucm.es/Tools/sias.html).
Mentions: It thus appears that GH46 chitosanases from actinobacteria are rather homogenous at the primary sequence level, being grouped essentially in one large cluster A, while chitosanases from Firmicutes (Bacillus and related genera) fall into two distinct groups, one of which (cluster B) is relatively closer to the actinobacterial proteins than the other (cluster D). This is illustrated in Figure 2, showing the percentages of identity and similarity among the sequences of the catalytic modules of the best-characterized chitosanases from each cluster.

Bottom Line: Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan.Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level.This review is focused on the taxonomic distribution of GH46 proteins, their multi-modular character, the structure-function relationships and their biological functions in the host organisms.

View Article: PubMed Central - PubMed

Affiliation: Biologie, Faculté des Sciences, Université de Sherbrooke, 2500, boul. de l'Université, Sherbrooke, QC J1K 2R1, Canada. Pascal.Viens@USherbrooke.ca.

ABSTRACT
Chitosanases, enzymes that catalyze the endo-hydrolysis of glycolytic links in chitosan, are the subject of numerous studies as biotechnological tools to generate low molecular weight chitosan (LMWC) or chitosan oligosaccharides (CHOS) from native, high molecular weight chitosan. Glycoside hydrolases belonging to family GH46 are among the best-studied chitosanases, with four crystallography-derived structures available and more than forty enzymes studied at the biochemical level. They were also subjected to numerous site-directed mutagenesis studies, unraveling the molecular mechanisms of hydrolysis. This review is focused on the taxonomic distribution of GH46 proteins, their multi-modular character, the structure-function relationships and their biological functions in the host organisms.

Show MeSH
Related in: MedlinePlus